PROSITE documentation PDOC51913HARE-type HTH domain profile
Human ASXL proteins, orthologs of Drosophila Additional Sex combs, have been implicated in conjunction with TET2 as a major target for mutations and translocations leading to a wide range of myeloid leukemias, related myelodysplastic conditions (ASXL1 and ASXL2) and the Bohring-Opitz syndrome, a developmental disorder (ASXL1). Most animal ASXL proteins (except the Drosophila Asx protein) contain an N-terminal domain that is also found in several other eukaryotic chromatin proteins (including Arabidopsis HB1), diverse restriction endonucleases and DNA glycosylases, the RNA polymerase delta subunit of Gram-positive bacteria and certain bacterial proteins that combine features of the RNA polymerase α-subunit and sigma factors. This domain adopts the winged helix-turn-helix fold and is predicted to bind DNA. It has been named HARE-type HTH, for HB1, ASXL, restriction endonuclease, based on the proteins in which it was detected [1,2].
The HARE-type HTH domain consists of four α-helices (helices I, II, III, and IV) and an antiparallel β-sheet composed of three short β-strands at the top of a "twisted tripod" formed by helices II, III, and IV (see <PDB:2KRC>) [2].
The profile we developed covers the entire HARE-type HTH domain.
Last update:January 2020 / First entry.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Aravind L. Iyer L.M. |
| Title | The HARE-HTH and associated domains: novel modules in the coordination of epigenetic DNA and protein modifications. | |
| Source | Cell. Cycle. 11:119-131(2012). | |
| PubMed ID | 22186017 | |
| DOI | 10.4161/cc.11.1.18475 |
| 2 | Authors | Motackova V. Sanderova H. Zidek L. Novacek J. Padrta P. Svenkova A. Korelusova J. Jonak J. Krasny L. Sklenar V. |
| Title | Solution structure of the N-terminal domain of Bacillus subtilis delta subunit of RNA polymerase and its classification based on structural homologs. | |
| Source | Proteins 78:1807-1810(2010). | |
| PubMed ID | 20310067 | |
| DOI | 10.1002/prot.22708 |
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